A novel low molecular weight phospholipase D from Streptomyces sp. CS684.
With the aim of isolating economically viable enzymes from a microbial source, a novel phospholipase D (PLD) was purified from Streptomyces sp. CS684 (PLD(684)). PLD(684) had molecular weight of 29 kDa, which makes it the second smallest PLD reported so far. The enzyme activity was optimum at pH 6 and 45 degrees C, and enhanced by various detergents. It was stable from pH 7 to 9 and at or below 45 degrees C when assayed after 40 h and 2h, respectively. The K(m) and V(max) values for phosphatidylcholine were 1.16 mM and 1453.74 micromol min(-1)mg(-1), respectively. It catalyzed the transphosphatidylation of glycerol, but not that of l-serine, myo-inositol or ethanolamine. Low molecular weight PLD(684) with transphosphatidylation activity may be utilized in the industrial production of rare and commercially important phospholipids.
Simkhada
Jaya Ram
JR
Department of Pharmacy, College of Pharmacy, Chosun University, Dong-gu, Gwangju, Republic of Korea.
Lee
Hyo Jeong
HJ
Jang
So Young
SY
Kim
Ji Hyun
JH
Lee
Hei Chan
HC
Sohng
Jae Kyung
JK
Yoo
Jin Cheol
JC
D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010739:Phospholipase D / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D010743:Phospholipids / Q000737:chemistry*; D013302:Streptomyces / Q000378:metabolism*; D013696:Temperature
D010743:Phospholipids; D010739:Phospholipase D